2fr0
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2fr0.gif|left|200px]] | [[Image:2fr0.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2fr0", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2fr0| PDB=2fr0 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''The first ketoreductase of the erythromycin synthase (crystal form 1)''' | '''The first ketoreductase of the erythromycin synthase (crystal form 1)''' | ||
| Line 23: | Line 20: | ||
==Reference== | ==Reference== | ||
The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases., Keatinge-Clay AT, Stroud RM, Structure. 2006 Apr;14(4):737-48. Epub 2006 Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16564177 16564177] | The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases., Keatinge-Clay AT, Stroud RM, Structure. 2006 Apr;14(4):737-48. Epub 2006 Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16564177 16564177] | ||
| - | [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]] | ||
[[Category: Saccharopolyspora erythraea]] | [[Category: Saccharopolyspora erythraea]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Keatinge-Clay, A T.]] | [[Category: Keatinge-Clay, A T.]] | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
| - | [[Category: | + | [[Category: Short chain dehydrogenase/reductase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:12:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:12, 4 May 2008
The first ketoreductase of the erythromycin synthase (crystal form 1)
Overview
The structure of the ketoreductase (KR) from the first module of the erythromycin synthase with NADPH bound was solved to 1.79 A resolution. The 51 kDa domain has two subdomains, each similar to a short-chain dehydrogenase/reductase (SDR) monomer. One subdomain has a truncated Rossmann fold and serves a purely structural role stabilizing the other subdomain, which catalyzes the reduction of the beta-carbonyl of a polyketide and possibly the epimerization of an alpha-substituent. The structure enabled us to define the domain boundaries of KR, the dehydratase (DH), and the enoylreductase (ER). It also constrains the three-dimensional organization of these domains within a module, revealing that KR does not make dimeric contacts across the 2-fold axis of the module. The quaternary structure elucidates how substrates are shuttled between the active sites of polyketide synthases (PKSs), as well as related fatty acid synthases (FASs), and suggests how domains can be swapped to make hybrid synthases that produce novel polyketides.
About this Structure
2FR0 is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.
Reference
The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases., Keatinge-Clay AT, Stroud RM, Structure. 2006 Apr;14(4):737-48. Epub 2006 Mar 23. PMID:16564177 Page seeded by OCA on Sun May 4 04:12:51 2008
